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1.
Appl Clin Inform ; 13(4): 901-909, 2022 08.
Artículo en Inglés | MEDLINE | ID: mdl-36170880

RESUMEN

BACKGROUND: Chronic kidney disease (CKD) is a major global health problem that affects approximately one in 10 adults. Up to 90% of individuals with CKD go undetected until its progression to advanced stages, invariably leading to death in the absence of treatment. The project aims to fill information gaps around the burden of CKD in the Western Australian (WA) population, including incidence, prevalence, rate of progression, and economic cost to the health system. METHODS: Given the sensitivity of the information involved, the project employed a privacy preserving record linkage methodology to link data from four major pathology providers in WA to hospital records, to establish a CKD registry with continuous medical record for individuals with biochemical specification for CKD. This method uses encrypted personal identifying information in a probability-based linkage framework (Bloom filters) to help mitigate risk while maximizing linkage quality. RESULTS: The project developed interoperable technology to create a transparent CKD data catalogue which is linkable to other datasets. This technology has been designed to support the aspirations of the research program to provide linked de-identified pathology, morbidity, and mortality data that can be used to derive insights to enable better CKD patient outcomes. The cohort includes over 1 million individuals with creatinine results over the period 2002 to 2021. CONCLUSION: Using linked data from across the care continuum, researchers are able to evaluate the effectiveness of service delivery and provide evidence for policy and program development. The CKD registry will enable an innovative review of the epidemiology of CKD in WA. Linking pathology records can identify cases of CKD that are missed in the early stages due to disaggregation of results, enabling identification of at-risk populations that represent targets for early intervention and management.


Asunto(s)
Privacidad , Insuficiencia Renal Crónica , Adulto , Australia , Creatinina , Humanos , Registro Médico Coordinado/métodos , Insuficiencia Renal Crónica/diagnóstico , Insuficiencia Renal Crónica/epidemiología , Insuficiencia Renal Crónica/terapia , Web Semántica
2.
PLoS One ; 5(11): e15042, 2010 Nov 29.
Artículo en Inglés | MEDLINE | ID: mdl-21124783

RESUMEN

The enzymatic activity of Helicobacter pylori's urease neutralises stomach acidity, thereby promoting infection by this pathogen. Urease protein has also been found to interact with host cells in vitro, although this property's possible functional importance has not been studied in vivo. To test for a role of the urease surface in the host/pathogen interaction, surface exposed loops that display high thermal mobility were targeted for inframe insertion mutagenesis. H. pylori expressing urease with insertions at four of eight sites tested retained urease activity, which in three cases was at least as stable as was wild-type urease at pH 3. Bacteria expressing one of these four mutant ureases, however, failed to colonise mice for even two weeks, and a second had reduced bacterial titres after longer term (3 to 6 months) colonisation. These results indicate that a discrete surface of the urease complex is important for H. pylori persistence during gastric colonisation. We propose that this surface interacts directly with host components important for the host-pathogen interaction, immune modulation or other actions that underlie H. pylori persistence in its special gastric mucosal niche.


Asunto(s)
Adhesión Bacteriana , Proteínas Bacterianas/metabolismo , Helicobacter pylori/enzimología , Ureasa/metabolismo , Animales , Proteínas Bacterianas/química , Proteínas Bacterianas/genética , Sitios de Unión/genética , Estabilidad de Enzimas , Ácido Gástrico/metabolismo , Mucosa Gástrica/metabolismo , Mucosa Gástrica/microbiología , Helicobacter pylori/genética , Interacciones Huésped-Patógeno , Concentración de Iones de Hidrógeno , Ratones , Ratones Endogámicos C57BL , Modelos Moleculares , Mutación , Estructura Terciaria de Proteína , Estómago/microbiología , Propiedades de Superficie , Ureasa/química , Ureasa/genética
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